This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Simmons, D L
Right arrow Articles by Erikson, R L
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Simmons, D L
Right arrow Articles by Erikson, R L

 Previous Article  |  Next Article 

Mol Cell Biol. 1992 September; 12(9): 4164-4169

Identification of an early-growth-response gene encoding a novel putative protein kinase.

D L Simmons, B G Neel, R Stevens, G Evett and R L Erikson

Department of Chemistry, Brigham Young University, Provo, Utah 84602.

ABSTRACT

Early-growth-response genes, also known as immediate-early genes, play important roles in regulating cell proliferation. We have identified a new type of early-growth-response gene product, a 77,811-Da putative serine/threonine kinase, which is highly inducible by serum and phorbol ester. mRNA encoding this putative kinase is markedly elevated within 1 h after treatment with mitogen, and this induction is synergistically increased by cycloheximide. Dexamethasone blocks serum induction of the kinase mRNA, as does transformation by v-Ki-ras. The kinase mRNA was detected in mouse brain, lung, and heart. This new putative kinase, which we term Snk, for serum-inducible kinase, showed similarity in its proposed catalytic domain to many other protein kinases; however, no other kinase showed enough sequence similarity with Snk to suggest the existence of a common function. Hence, Snk represents a new type of protein kinase involved in the early mitogenic response whose activity is transcriptionally and posttranscriptionally regulated.

Mol Cell Biol. 1992 September; 12(9): 4164-4169




This article has been cited by other articles:

  • Horner, T. J., Lai, W. S., Stumpo, D. J., Blackshear, P. J. (2009). Stimulation of Polo-Like Kinase 3 mRNA Decay by Tristetraprolin. Mol. Cell. Biol. 29: 1999-2010 [Abstract] [Full Text]  
  • Inglis, K. J., Chereau, D., Brigham, E. F., Chiou, S.-S., Schobel, S., Frigon, N. L., Yu, M., Caccavello, R. J., Nelson, S., Motter, R., Wright, S., Chian, D., Santiago, P., Soriano, F., Ramos, C., Powell, K., Goldstein, J. M., Babcock, M., Yednock, T., Bard, F., Basi, G. S., Sham, H., Chilcote, T. J., McConlogue, L., Griswold-Prenner, I., Anderson, J. P. (2009). Polo-like Kinase 2 (PLK2) Phosphorylates {alpha}-Synuclein at Serine 129 in Central Nervous System. J. Biol. Chem. 284: 2598-2602 [Abstract] [Full Text]  
  • Wang, L., Gao, J., Dai, W., Lu, L. (2008). Activation of Polo-like Kinase 3 by Hypoxic Stresses. J. Biol. Chem. 283: 25928-25935 [Abstract] [Full Text]  
  • Yang, Y., Bai, J., Shen, R., Brown, S. A.N., Komissarova, E., Huang, Y., Jiang, N., Alberts, G. F., Costa, M., Lu, L., Winkles, J. A., Dai, W. (2008). Polo-like Kinase 3 Functions as a Tumor Suppressor and Is a Negative Regulator of Hypoxia-Inducible Factor-1{alpha} under Hypoxic Conditions. Cancer Res. 68: 4077-4085 [Abstract] [Full Text]  
  • Schmit, T. L, Ahmad, N. (2008). Regulation of Mitosis via Mitotic Kinases: New Opportunities for Cancer Management. aacredbook 2008: 133-150 [Abstract] [Full Text]  
  • Schmit, T. L., Ahmad, N. (2007). Regulation of mitosis via mitotic kinases: new opportunities for cancer management. Molecular Cancer Therapeutics 6: 1920-1931 [Abstract] [Full Text]  
  • Syed, N., Smith, P., Sullivan, A., Spender, L. C., Dyer, M., Karran, L., O'Nions, J., Allday, M., Hoffmann, I., Crawford, D., Griffin, B., Farrell, P. J., Crook, T. (2006). Transcriptional silencing of Polo-like kinase 2 (SNK/PLK2) is a frequent event in B-cell malignancies. Blood 107: 250-256 [Abstract] [Full Text]  
  • Yogosawa, S., Hatakeyama, S., Nakayama, K. I., Miyoshi, H., Kohsaka, S., Akazawa, C. (2005). Ubiquitylation and Degradation of Serum-inducible Kinase by hVPS18, a RING-H2 Type Ubiquitin Ligase. J. Biol. Chem. 280: 41619-41627 [Abstract] [Full Text]  
  • Wang, J.-C., Derynck, M. K., Nonaka, D. F., Khodabakhsh, D. B., Haqq, C., Yamamoto, K. R. (2004). From The Cover: Chromatin immunoprecipitation (ChIP) scanning identifies primary glucocorticoid receptor target genes. Proc. Natl. Acad. Sci. USA 101: 15603-15608 [Abstract] [Full Text]  
  • Yuan, J.-H., Feng, Y., Fisher, R. H., Maloid, S., Longo, D. L., Ferris, D. K. (2004). Polo-Like Kinase 1 Inactivation Following Mitotic DNA Damaging Treatments Is Independent of Ataxia Telangiectasia Mutated Kinase. Mol Cancer Res 2: 417-426 [Abstract] [Full Text]  
  • Ando, K., Ozaki, T., Yamamoto, H., Furuya, K., Hosoda, M., Hayashi, S., Fukuzawa, M., Nakagawara, A. (2004). Polo-like Kinase 1 (Plk1) Inhibits p53 Function by Physical Interaction and Phosphorylation. J. Biol. Chem. 279: 25549-25561 [Abstract] [Full Text]  
  • Kho, P. S., Wang, Z., Zhuang, L., Li, Y., Chew, J.-L., Ng, H.-H., Liu, E. T., Yu, Q. (2004). p53-regulated Transcriptional Program Associated with Genotoxic Stress-induced Apoptosis. J. Biol. Chem. 279: 21183-21192 [Abstract] [Full Text]  
  • Pak, D. T. S., Sheng, M. (2003). Targeted Protein Degradation and Synapse Remodeling by an Inducible Protein Kinase. Science 302: 1368-1373 [Abstract] [Full Text]  
  • Ma, S., Charron, J., Erikson, R. L. (2003). Role of Plk2 (Snk) in Mouse Development and Cell Proliferation. Mol. Cell. Biol. 23: 6936-6943 [Abstract] [Full Text]  
  • Burns, T. F., Fei, P., Scata, K. A., Dicker, D. T., El-Deiry, W. S. (2003). Silencing of the Novel p53 Target Gene Snk/Plk2 Leads to Mitotic Catastrophe in Paclitaxel (Taxol)-Exposed Cells. Mol. Cell. Biol. 23: 5556-5571 [Abstract] [Full Text]  
  • Ma, S., Liu, M.-A., Yuan, Y.-L. O., Erikson, R. L. (2003). The Serum-Inducible Protein Kinase Snk Is a G1 Phase Polo-Like Kinase That Is Inhibited by the Calcium- and Integrin-Binding Protein CIB. Mol Cancer Res 1: 376-384 [Abstract] [Full Text]  
  • Maiyar, A. C., Leong, M. L.L., Firestone, G. L. (2003). Importin-alpha Mediates the Regulated Nuclear Targeting of Serum- and Glucocorticoid-inducible Protein Kinase (Sgk) by Recognition of a Nuclear Localization Signal in the Kinase Central Domain. Mol. Biol. Cell 14: 1221-1239 [Abstract] [Full Text]  
  • Yarm, F. R. (2002). Plk Phosphorylation Regulates the Microtubule-Stabilizing Protein TCTP. Mol. Cell. Biol. 22: 6209-6221 [Abstract] [Full Text]  
  • Wang, Q., Xie, S., Chen, J., Fukasawa, K., Naik, U., Traganos, F., Darzynkiewicz, Z., Jhanwar-Uniyal, M., Dai, W. (2002). Cell Cycle Arrest and Apoptosis Induced by Human Polo-Like Kinase 3 Is Mediated through Perturbation of Microtubule Integrity. Mol. Cell. Biol. 22: 3450-3459 [Abstract] [Full Text]  
  • Yamashita, Y., Kajigaya, S., Yoshida, K., Ueno, S., Ota, J., Ohmine, K., Ueda, M., Miyazato, A., Ohya, K.-i., Kitamura, T., Ozawa, K., Mano, H. (2001). Sak Serine-Threonine Kinase Acts as an Effector of Tec Tyrosine Kinase. J. Biol. Chem. 276: 39012-39020 [Abstract] [Full Text]  
  • Cogswell, J. P., Brown, C. E., Bisi, J. E., Neill, S. D. (2000). Dominant-Negative Polo-like Kinase 1 Induces Mitotic Catastrophe Independent of cdc25C Function. Cell Growth Differ. 11: 615-623 [Abstract] [Full Text]  
  • Conn, C. W., Hennigan, R. F., Dai, W., Sanchez, Y., Stambrook, P. J. (2000). Incomplete Cytokinesis and Induction of Apoptosis by Overexpression of the Mammalian Polo-Like Kinase, Plk3. Cancer Res. 60: 6826-6831 [Abstract] [Full Text]  
  • Song, S., Grenfell, T. Z., Garfield, S., Erikson, R. L., Lee, K. S. (2000). Essential Function of the Polo Box of Cdc5 in Subcellular Localization and Induction of Cytokinetic Structures. Mol. Cell. Biol. 20: 286-298 [Abstract] [Full Text]  
  • Lee, K. S., Song, S., Erikson, R. L. (1999). The polo-box-dependent induction of ectopic septal structures by a mammalian polo kinase, Plk, in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 96: 14360-14365 [Abstract] [Full Text]  
  • KUMAR, J. M., BROOKS, D. P., OLSON, B. A., LAPING, N. J. (1999). Sgk, a Putative Serine/Threonine Kinase, Is Differentially Expressed in the Kidney of Diabetic Mice and Humans. J. Am. Soc. Nephrol. 10: 2488-2494 [Abstract] [Full Text]  
  • Glover, D. M., Hagan, I. M., Tavares, A. A.M. (1998). Polo-like kinases: a team that plays throughout mitosis. Genes Dev. 12: 3777-3787 [Full Text]  
  • Lee, K. S., Grenfell, T. Z., Yarm, F. R., Erikson, R. L. (1998). Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk. Proc. Natl. Acad. Sci. USA 95: 9301-9306 [Abstract] [Full Text]  
  • Logarinho, E, Sunkel, C. (1998). The Drosophila POLO kinase localises to multiple compartments of the mitotic apparatus and is required for the phosphorylation of MPM2 reactive epitopes. J. Cell Sci. 111: 2897-2909 [Abstract]  
  • Ouyang, B., Pan, H., Lu, L., Li, J., Stambrook, P., Li, B., Dai, W. (1997). Human Prk Is a Conserved Protein Serine/Threonine Kinase Involved in Regulating M Phase Functions. J. Biol. Chem. 272: 28646-28651 [Abstract] [Full Text]  
  • Waldegger, S., Barth, P., Raber, G., Lang, F. (1997). Cloning and characterization of a putative human serine/threonine protein kinase transcriptionally modified during anisotonic and isotonic alterations of cell volume. Proc. Natl. Acad. Sci. USA 94: 4440-4445 [Abstract] [Full Text]  
  • Maiyar, A. C., Phu, P. T., Huang, A. J., Firestone, G. L. (1997). Repression of Glucocorticoid Receptor Transactivation and DNA Binding of a Glucocorticoid Response Element within the Serum/Glucocorticoid-Inducible Protein Kinase (sgk) Gene Promoter by the p53 Tumor Suppressor Protein. Mol. Endocrinol. 11: 312-329 [Abstract] [Full Text]  
  • Li, B., Ouyang, B., Pan, H., Reissmann, PeterT., Slamon, DennisJ., Arceci, R., Lu, L., Dai, W. (1996). prk, a Cytokine-inducible Human Protein Serine/Threonine Kinase Whose Expression Appears to be Down-regulated in Lung Carcinomas. J. Biol. Chem. 271: 19402-19408 [Abstract] [Full Text]  
  • Maiyar, A. C., Huang, A. J., Phu, P. T., Cha, H. H., Firestone, G. L. (1996). p53 Stimulates Promoter Activity of the sgk Serum/Glucocorticoid-inducible Serine/Threonine Protein Kinase Gene in Rodent Mammary Epithelial Cells. J. Biol. Chem. 271: 12414-12422 [Abstract] [Full Text]  
  • Ohkura, H, Hagan, I M, Glover, D M (1995). The conserved Schizosaccharomyces pombe kinase plo1, required to form a bipolar spindle, the actin ring, and septum, can drive septum formation in G1 and G2 cells.. Genes Dev. 9: 1059-1073 [Abstract]  
  • Donohue, P. J., Alberts, G. F., Guo, Y., Winkles, J. A. (1995). Identification by Targeted Differential Display of an Immediate Early Gene Encoding a Putative Serine/Threonine Kinase. J. Biol. Chem. 270: 10351-10357 [Abstract] [Full Text]  
  • Golsteyn, R., Schultz, S., Bartek, J, Ziemiecki, A, Ried, T, Nigg, E. (1994). Cell cycle analysis and chromosomal localization of human Plk1, a putative homologue of the mitotic kinases Drosophila polo and Saccharomyces cerevisiae Cdc5. J. Cell Sci. 107: 1509-1517 [Abstract]  
  • Xie, S., Wang, Q., Wu, H., Cogswell, J., Lu, L., Jhanwar-Uniyal, M., Dai, W. (2001). Reactive Oxygen Species-induced Phosphorylation of p53 on Serine 20 Is Mediated in Part by Polo-like Kinase-3. J. Biol. Chem. 276: 36194-36199 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»